Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P50583 (asymmetrical)
 12,197 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Electron spin resonance study of Mn (II) binding to chromatin and derivatives, including core particles, shows that Mn (II) is a good probe for testing the overall electrostatic balance of the nucleoproteic complex as well as DNA accessibility. Experimental results are in good agreement with a recent model proposed (Mirzabekov A. D. and Rich A. (1979) Proc. Natl. Acad. Sci. USA 76, 1118-1121), for the core particle, in which an asymmetrical shielding of DNA by the protein core is assumed. Furthermore, it was found that the histone H1 hinders a number of charges on the linker DNA in a proportion equal to the net positive charge of the histone itself. This result is interpreted as due to a tighter interaction between the linker DNA and the core histones in the presence of histone H1.
 ...
PMID:Experimental evidence for asymmetrical shielding of nucleosomal DNA by histones. 23 Apr 66

We have reconstituted oligonucleosome complexes containing histone H1 starting from a synthetic DNA template, consisting of 12 tandemly arranged 208-base pair fragments of the 5 S rRNA gene, purified HeLa histone octamers, and histone H1. A ratio of histone H1 per histone octamer used in the reconstitution (0.8-0.9 mol of histone H1/mol of histone octamer) similar to that observed in vivo was used. The reconstituted chromatin complexes exhibit a salt-dependent folding, which is almost indistinguishable from that exhibited by chromatin fragments obtained from nuclease digestion of native chromatin. The folding of this reconstituted chromatin complex seems to be rather independent of the symmetrical or asymmetrical position occupied by H1 in the individual nucleosomes. Binding of histone H1 to the oligonucleosome complexes, under the stoichiometric binding conditions used, had no inhibitory effect on the transcriptional potential of these complexes.
 ...
PMID:Folding of chromatin in the presence of heterogeneous histone H1 binding to nucleosomes. 956 81